ArticleThe Journal of cell biology2000
Dynamic localization of protein phosphatase type 1 in the mitotic cell cycle of Saccharomyces cerevisiae.
Article in The Journal of cell biology, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.
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Who cites it
37 citing papers in PubMed.
- Single-molecule tracking reveals the dynamic turnover of Ipl1 at the kinetochores inLife science alliance · 2025Article
- Glycogen synthase activity inmSphere · 2024Article
- Remodeling of the secretory pathway is coordinated withiScience · 2024Article
- Analog-sensitive Cdk1 as a tool to study mitotic exit: protein phosphatase 1 is required downstream from Cdk1 inactivation in budding yeast.Chromosome research : an international journal on the molecular, supramolecular and evolutionary aspects of chromosome biology · 2023Article
- The phosphatase Glc7 controls the eisosomal response to starvation via post-translational modification of Pil1.Journal of cell science · 2023Article
- Exit from Mitosis in Budding Yeast: Protein Phosphatase 1 is Required Downstream from Cdk1 Inactivation.Research square · 2023Article
- Stage-Specific Genetic Interaction betweenInternational journal of molecular sciences · 2022Article
- Reg1 and Snf1 regulate stress-induced relocalization of protein phosphatase-1 to cytoplasmic granules.The FEBS journal · 2021Article
- Co-option of Plasmodium falciparum PP1 for egress from host erythrocytes.Nature communications · 2020Article
- Article
- The Pch2 AAA+ ATPase promotes phosphorylation of the Hop1 meiotic checkpoint adaptor in response to synaptonemal complex defects.Nucleic acids research · 2016Article
- PP1-Dependent Formin Bnr1 Dephosphorylation and Delocalization from a Cell Division Site.PloS one · 2016Article
- An integrated overview of spatiotemporal organization and regulation in mitosis in terms of the proteins in the functional supercomplexes.Frontiers in microbiology · 2014Review
- Article
- The budding yeast Cdc48(Shp1) complex promotes cell cycle progression by positive regulation of protein phosphatase 1 (Glc7).PloS one · 2013Article
- Temperature-sensitive ipl1-2/Aurora B mutation is suppressed by mutations in TOR complex 1 via the Glc7/PP1 phosphatase.Proceedings of the National Academy of Sciences of the United States of America · 2011Article
- Changes in Bni4 localization induced by cell stress in Saccharomyces cerevisiae.Journal of cell science · 2010Article
- Quantitative proteomic analysis of purified yeast kinetochores identifies a PP1 regulatory subunit.Genes & development · 2009Article
- Septins: molecular partitioning and the generation of cellular asymmetry.Cell division · 2009Article
- Regulation of Sli15/INCENP, kinetochore, and Cdc14 phosphatase functions by the ribosome biogenesis protein Utp7.The Journal of cell biology · 2008Article
Corrections and comments
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Authors and funding
2 authors.
Funding
Abstract
Protein phosphatase type I (PP1), encoded by the single essential gene GLC7 in Saccharomyces cerevisiae, functions in diverse cellular processes. To identify in vivo subcellular location(s) where these processes take place, we used a functional green fluorescent protein (GFP)-Glc7p fusion protein. Time-lapse fluorescence microscopy revealed GFP-Glc7p localizes predominantly in the nucleus throughout the mitotic cell cycle, with the highest concentrations in the nucleolus. GFP-Glc7p was also observed in a ring at the bud neck, which was dependent upon functional septins. Supporting a role for Glc7p in bud site selection, a glc7-129 mutant displayed a random budding pattern. In alpha-factor treated cells, GFP-Glc7p was located at the base of mating projections, again in a septin-dependent manner. At the start of anaphase, GFP-Glc7p accumulated at the spindle pole bodies and remained there until cytokinesis. After anaphase, GFP-Glc7p became concentrated in a ring that colocalized with the actomyosin ring. A GFP-Glc7-129 fusion was defective in localizing to the bud neck and SPBs. Together, these results identify sites of Glc7p function and suggest Glc7p activity is regulated through dynamic changes in its location.
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